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Biallelic loss-of-function variants in MFSD8 cause autosomal recessive neuronal ceroid lipofuscinosis 7 (CLN7) (MONDO_0012588). Two unrelated human patients harbored pathogenic MFSD8 variants, including a compound heterozygous two-nucleotide deletion c.136_137del (p.Met46ValfsTer22) (PMID:35154277) and a homozygous whole-gene deletion confirmed by CNV-seq and qPCR (PMID:35917699). Clinically, affected individuals presented with seizures, aggressive behavior, ataxia, sleep disturbances, and rhabdomyolysis in the context of sepsis. A domestic shorthair cat with a homozygous frameshift in MFSD8 exhibited abnormal posture and diffuse brain dysfunction, supporting a conserved role in neurodegeneration.
Functional experiments demonstrate that CLN7 is a polytopic lysosomal membrane protein requiring an N-terminal dileucine motif for correct lysosomal targeting; missense mutations (e.g., p.Thr294Lys, p.Pro412Leu) enhance proteolytic cleavage and mislocalize CLN7 to the plasma membrane (PMID:20406422). In Cln7 knockout mouse embryonic fibroblasts, quantitative proteomics revealed depletion of soluble lysosomal proteins (including CLN5) and impaired mTORC1 reactivation under starvation, indicating a loss-of-function mechanism for CLN7 disease (PMID:29514215). These data provide limited genetic evidence with strong concordant functional data linking MFSD8 deficiency to CLN7 pathogenesis. Further natural history and segregation studies are needed to move beyond the current evidence cap.
Key Take-home: MFSD8 loss-of-function variants are a limited but emerging cause of autosomal recessive CLN7, with supportive functional and animal-model data underpinning diagnostic and research applications.
Gene–Disease AssociationLimited2 unrelated probands with biallelic MFSD8 frameshift and deletion variants and supportive animal model data Genetic EvidenceLimited2 human probands with confirmed biallelic LoF MFSD8 variants ([PMID:35154277],[PMID:35917699]) Functional EvidenceModerateMutational analyses show disrupted lysosomal targeting and enhanced proteolytic cleavage of CLN7 ([PMID:20406422]); Cln7 knockout MEFs exhibit lysosomal protein depletion and impaired mTORC1 reactivation ([PMID:29514215]) |